X-ray diffraction
1.9Å resolution

Crystal Structure of human ATIC in complex with XMP


Function and Biology Details

Reactions catalysed:
IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Bifunctional purine biosynthesis protein ATIC Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 592 amino acids
Theoretical weight: 64.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P31939 (Residues: 1-592; Coverage: 100%)
Gene names: ATIC, OK/SW-cl.86, PURH
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 77.52Å b: 93.56Å c: 179.88Å
α: 90° β: 91.09° γ: 90°
R R work R free
0.211 0.211 0.249
Expression system: Escherichia coli